| Abstract
| - Conformational analysis of peptides containingcis-3-hydroxy-d-proline (d-cis-3-Hyp) by NMR studies revealed that the 3-hydroxyl group in this amino acid plays asignificant role in the overall three-dimensional structuresof the peptides. When the d-cis-3-Hyp had its 3-hydroxylgroup protected as the benzyl (Bn) ether, the peptidedisplayed a β-hairpin structure in both CDCl3 and DMSO-d6. Even after the removal of the Bn group, the resultingdeprotected compound retained the same structure as in theprotected version in CDCl3. However, in polar solventDMSO-d6, the C-terminal strand of the hydroxyl-deprotectedpeptide flipped to the side of the hydroxyl group, breakingthe hairpin to form a pseudo β-turn-like nine-membered ringstructure involving an intramolecular hydrogen bond between LeuNH → HypC3-OH.
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